Proteins contain polypeptide sequences that encode the protein's functional, stable, native three-dimensional state. In certain circumstances proteins misfold or are cut into peptides which then aggregate into a structure called amyloid fibrils. Regardless of the underlying protein or peptide, amyloid fibrils have a characteristic structure composed predominantly of beta-sheets which associate into an elongated fibular form. Amyloid fibrils are associated with a large number of neurodegenerative diseases, which include, but are not limited to, Alzheimer's and Parkinson's disease. See: Chin, F. and Dobson, C M. (2006) Protein misfolding, functional amyloid and human disease. Ann. Rev. Biochem, 75, 333-366. There are also other debilitating diseases where amyloid fibrils form deposits in areas outside of the central nervous system. These include intra-articular spaces as in the case of prolonged-renal dialysis associated amyloidosis. See: Eakin, C. M. and Miranker, A. D., “From chance to frequent encounters: origins of β2-microglobulin fibrillogenesis,” Biochimica Biphysica Acta 1753, 92-99 (2005). Diseases that are linked to the presence of amyloid fibrils include, but are not limited to: type 2 diabetes mellitus, transmissible spongiform encephalopathy (e.g., Bovine Spongiform Encephalopathy aka “Mad Cow Disease”), Huntington's disease, medullary carcinoma of the thyroid, cardiac arrhythmias, atherosclerosis, rheumatoid arthritis, aortic medial amyloid, prolactinomas, familial amyloid polyneuropathy, hereditary non-neuropathic systemic amyloidosis, dialysis related amyloidosis. Finnish amyloidosis, lattice corneal dystrophy, cerebral amyloid angiopathy, cerebral amyloid angiopathy (Icelandic type), systemic AL amyloidosis, yeast prions, sporadic inclusion body myositis, pheochromocytoma, osteomyelitis and multiple myeloma. At present there is no cure for amyloid-related diseases. Thus, techniques for treating amyloid-related diseases in the body are needed.